The interaction between the active chips mounted and the same base plate is considered as a thermoelectrical coupling effect.An approach to coupling effect analysis of a multi-chip system is presented with IGBT as a s...The interaction between the active chips mounted and the same base plate is considered as a thermoelectrical coupling effect.An approach to coupling effect analysis of a multi-chip system is presented with IGBT as a sample.Finite element method is used to evaluate the temperature distribution in power modules.The precise electrothermal model is obtained by fitting the curve of transient thermal impedance with a finite series of exponential terms,in which,the thermal-coupling effect among chips is considered as a prediction of the highest transient temperature of the chips.This model can be used in many thermal monitoring systems.Both ANSYS and PSPICE si- mulation software have been employed,and the simulation results agree with the experimental ones very well.展开更多
The small GTPase Rap1 induces integrin activation via an inside-out signaling pathway mediated by the Rapl-interacting adaptor mol- ecule （RIAM）. Blocking this pathway may suppress tumor metastasis and other disease...The small GTPase Rap1 induces integrin activation via an inside-out signaling pathway mediated by the Rapl-interacting adaptor mol- ecule （RIAM）. Blocking this pathway may suppress tumor metastasis and other diseases that are related to hyperactive integrins. However, the molecular basis for the specific recognition of RIAM by Rap1 remains largely unknown. Herein we present the crystal structure of an active, GTP-bound GTPase domain of Rap1 in complex with the Ras association （RA）-pleckstrin homology （PH） structural module of RIAM at 1.65 A. The structure reveals that the recognition of RIAM by Rap1 is governed by side-chain interactions. Several side chains are critical in determining specificity of this recognition, particularly the Lys31 residue in Rap1 that is oppositely charged compared with the Glu31/Asp31 residue in other Ras GTPases. Lys31 forms a salt bridge with RIAM residue Glu212, making it the key specificity determinant of the interaction. We also show that disruption of these interactions results in reduction of Rapl：RIAM association, leadingto a loss of co-clustering and cell adhesion. Our findings elucidate the molecular mechanism by which RIAM med- iates Rapl-induced integrin activation. The crystal structure also offers new insight into the structural basis for the specific recruitment of RA-PH module-containing effector proteins by their smaU GTPase partners.展开更多
文摘The interaction between the active chips mounted and the same base plate is considered as a thermoelectrical coupling effect.An approach to coupling effect analysis of a multi-chip system is presented with IGBT as a sample.Finite element method is used to evaluate the temperature distribution in power modules.The precise electrothermal model is obtained by fitting the curve of transient thermal impedance with a finite series of exponential terms,in which,the thermal-coupling effect among chips is considered as a prediction of the highest transient temperature of the chips.This model can be used in many thermal monitoring systems.Both ANSYS and PSPICE si- mulation software have been employed,and the simulation results agree with the experimental ones very well.
文摘The small GTPase Rap1 induces integrin activation via an inside-out signaling pathway mediated by the Rapl-interacting adaptor mol- ecule （RIAM）. Blocking this pathway may suppress tumor metastasis and other diseases that are related to hyperactive integrins. However, the molecular basis for the specific recognition of RIAM by Rap1 remains largely unknown. Herein we present the crystal structure of an active, GTP-bound GTPase domain of Rap1 in complex with the Ras association （RA）-pleckstrin homology （PH） structural module of RIAM at 1.65 A. The structure reveals that the recognition of RIAM by Rap1 is governed by side-chain interactions. Several side chains are critical in determining specificity of this recognition, particularly the Lys31 residue in Rap1 that is oppositely charged compared with the Glu31/Asp31 residue in other Ras GTPases. Lys31 forms a salt bridge with RIAM residue Glu212, making it the key specificity determinant of the interaction. We also show that disruption of these interactions results in reduction of Rapl：RIAM association, leadingto a loss of co-clustering and cell adhesion. Our findings elucidate the molecular mechanism by which RIAM med- iates Rapl-induced integrin activation. The crystal structure also offers new insight into the structural basis for the specific recruitment of RA-PH module-containing effector proteins by their smaU GTPase partners.
